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Conserved domains on  [gi|122920638|pdb|2II3|G]
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Chain G, Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex

Protein Classification

lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex( domain architecture ID 1003376)

lipoamide acyltransferase component (E2) of branched-chain alpha-keto acid dehydrogenase complex that catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2)

CATH:  3.30.559.10
EC:  2.3.1.168
Gene Ontology:  GO:0043754|GO:0016407|GO:0031625|GO:0031405|GO:0009083

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02528 super family cl33511
2-oxoisovalerate dehydrogenase E2 component
 31-262 3.85e-119

2-oxoisovalerate dehydrogenase E2 component


The actual alignment was detected with superfamily member PLN02528:

Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 346.71  E-value: 3.85e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        31 DRTEPVKGFHKAMVKTMSAALKIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAASLGLLQFPILNASVD 110
Cdd:PLN02528 185 DKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFN 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G       111 ENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQIRSIFEIATELNRLQKLGSAGQLSTNDLIGGTFTLSNIGSIGGTYAK 190
Cdd:PLN02528 265 EETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGS 344

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2II3_G       191 PVILPPEVAIGALGTIKALPRFNEKGEVCKAQIMNVSWSADHRIIDGATVSRFSNLWKSYLENPAFMLLDLK 262
Cdd:PLN02528 345 PVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLMLHMR 416
 
Name Accession Description Interval E-value
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 31-262 3.85e-119

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 346.71  E-value: 3.85e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        31 DRTEPVKGFHKAMVKTMSAALKIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAASLGLLQFPILNASVD 110
Cdd:PLN02528 185 DKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFN 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G       111 ENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQIRSIFEIATELNRLQKLGSAGQLSTNDLIGGTFTLSNIGSIGGTYAK 190
Cdd:PLN02528 265 EETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGS 344

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2II3_G       191 PVILPPEVAIGALGTIKALPRFNEKGEVCKAQIMNVSWSADHRIIDGATVSRFSNLWKSYLENPAFMLLDLK 262
Cdd:PLN02528 345 PVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLMLHMR 416
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 47-258 7.68e-100

2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.


Pssm-ID: 425518 [Multi-domain]  Cd Length: 212  Bit Score: 290.21  E-value: 7.68e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G         47 MSAAL-KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIG 125
Cdd:pfam00198   1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        126 IAMDTEQGLIVPNVKNVQIRSIFEIATELNRLQKLGSAGQLSTNDLIGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGT 205
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
2II3_G        206 IKALPRFNEkGEVCKAQIMNVSWSADHRIIDGATVSRFSNLWKSYLENPAFML 258
Cdd:pfam00198 161 IRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 29-259 2.27e-47

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 165.05  E-value: 2.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G         29 GKDRTEPVKGFHKAMVKTMSAA-LKIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAASLGLLQFPILNA 107
Cdd:TIGR01348 316 GEVEEVDMSRIRKISGANLTRNwTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNA 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        108 SVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQIRSIFEIATELNRLQKLGSAGQLSTNDLIGGTFTLSNIGSIGGT 187
Cdd:TIGR01348 396 SLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGT 475

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2II3_G        188 YAKPVILPPEVAIgaLGTIKAL--PRFNEKgEVCKAQIMNVSWSADHRIIDGATVSRFSNLWKSYLENPAFMLL 259
Cdd:TIGR01348 476 AFTPIVNAPEVAI--LGVSKSGmePVWNGK-EFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
 
Name Accession Description Interval E-value
PLN02528 PLN02528
2-oxoisovalerate dehydrogenase E2 component
 31-262 3.85e-119

2-oxoisovalerate dehydrogenase E2 component


Pssm-ID: 215289 [Multi-domain]  Cd Length: 416  Bit Score: 346.71  E-value: 3.85e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        31 DRTEPVKGFHKAMVKTMSAALKIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAASLGLLQFPILNASVD 110
Cdd:PLN02528 185 DKTIPLRGFQRAMVKTMTAAAKVPHFHYVEEINVDALVELKASFQENNTDPTVKHTFLPFLIKSLSMALSKYPLLNSCFN 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G       111 ENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQIRSIFEIATELNRLQKLGSAGQLSTNDLIGGTFTLSNIGSIGGTYAK 190
Cdd:PLN02528 265 EETSEIRLKGSHNIGVAMATEHGLVVPNIKNVQSLSLLEITKELSRLQHLAAENKLNPEDITGGTITLSNIGAIGGKFGS 344

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2II3_G       191 PVILPPEVAIGALGTIKALPRFNEKGEVCKAQIMNVSWSADHRIIDGATVSRFSNLWKSYLENPAFMLLDLK 262
Cdd:PLN02528 345 PVLNLPEVAIIALGRIQKVPRFVDDGNVYPASIMTVTIGADHRVLDGATVARFCNEWKSYVEKPELLMLHMR 416
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 29-259 6.26e-104

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 312.14  E-value: 6.26e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        29 GKDRTEPVKGFHKAMVKTMSAAL-KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAASLGLLQFPILNA 107
Cdd:PRK11855 317 GEIETKPLSRIKKISAANLHRSWvTIPHVTQFDEADITDLEALRKQLKKEAEKAGVKLTMLPFFIKAVVAALKEFPVFNA 396

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G       108 SVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQIRSIFEIATELNRLQKLGSAGQLSTNDLIGGTFTLSNIGSIGGT 187
Cdd:PRK11855 397 SLDEDGDELTYKKYFNIGFAVDTPNGLVVPVIKDVDKKSLLEIAREIAELAKKARDGKLKPDDMQGGCFTISSLGGIGGT 476

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2II3_G       188 YAKPVILPPEVAIGALGTIKALPrFNEKGEVCKAQIMNVSWSADHRIIDGATVSRFSNLWKSYLENPAFMLL 259
Cdd:PRK11855 477 AFTPIINAPEVAILGVGKSQMKP-VWDGKEFVPRLMLPLSLSYDHRVIDGATAARFTNYLKQLLADPRRMLL 547
2-oxoacid_dh pfam00198
2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to ...
 47-258 7.68e-100

2-oxoacid dehydrogenases acyltransferase (catalytic domain); These proteins contain one to three copies of a lipoyl binding domain followed by the catalytic domain.


Pssm-ID: 425518 [Multi-domain]  Cd Length: 212  Bit Score: 290.21  E-value: 7.68e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G         47 MSAAL-KIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIG 125
Cdd:pfam00198   1 MTESKqTIPHFTLTDEVDVTELLALREELKEDAADEETKLTFLPFLVKAVALALKKFPELNASWDGEEGEIVYKKYVNIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        126 IAMDTEQGLIVPNVKNVQIRSIFEIATELNRLQKLGSAGQLSTNDLIGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGT 205
Cdd:pfam00198  81 IAVATPRGLIVPVIRNADRKSILEIAKEIKDLAERAREGKLKPEDLQGGTFTISNLGMFGVTFFTPIINPPQVAILGVGR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
2II3_G        206 IKALPRFNEkGEVCKAQIMNVSWSADHRIIDGATVSRFSNLWKSYLENPAFML 258
Cdd:pfam00198 161 IRKRPVVVD-GEIVVRKVMPLSLSFDHRVIDGAEAARFLNTLKELLENPELLL 212
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 8-260 1.91e-83

branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 255.49  E-value: 1.91e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G         8 PPPKPKDRTIPIPISKPPVFIGKDRTEPVKGFHKAMVKTMSAA-LKIPHFGYCDEVDLTELVKLREELKPIAfargIKLS 86
Cdd:PRK11856 165 AAAPAAAAAAAAAAAPPAAAAEGEERVPLSGMRKAIAKRMVESkREIPHFTLTDEVDVTALLALRKQLKAIG----VKLT 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        87 FMPFFLKAASLGLLQFPILNASVDEncQNITYKASHNIGIAMDTEQGLIVPNVKNVQIRSIFEIATELNRLQKLGSAGQL 166
Cdd:PRK11856 241 VTDFLIKAVALALKKFPELNASWDD--DAIVLKKYVNIGIAVATDGGLIVPVIRDADKKSLFELAREIKDLAEKAREGKL 318

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G       167 STNDLIGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGTIKALPRFNEkGEVCKAQIMNVSWSADHRIIDGATVSRFSNL 246
Cdd:PRK11856 319 KPEELQGGTFTISNLGMFGGDYFTPIINPPEVAILGVGAIVERPVVVD-GEIVVRKVMPLSLSFDHRVIDGADAARFLKA 397

                        250
                 ....*....|....
2II3_G       247 WKSYLENPAFMLLD 260
Cdd:PRK11856 398 LKELLENPALLLLE 411
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 51-253 4.65e-55

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 187.13  E-value: 4.65e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        51 LKIPHFGYCDEVDLTELVKLREELKPIAFAR--GIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAM 128
Cdd:PRK11854 424 VMIPHVTQFDKADITELEAFRKQQNAEAEKRklGVKITPLVFIMKAVAAALEQMPRFNSSLSEDGQRLTLKKYVNIGIAV 503

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G       129 DTEQGLIVPNVKNVQIRSIFEIATELNRLQKLGSAGQLSTNDLIGGTFTLSNIGSIGGTYAKPVILPPEVAIgaLGTIKA 208
Cdd:PRK11854 504 DTPNGLVVPVFKDVNKKGIIELSRELMDISKKARDGKLTAGDMQGGCFTISSIGGLGTTHFTPIVNAPEVAI--LGVSKS 581

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
2II3_G       209 L--PRFNEKgEVCKAQIMNVSWSADHRIIDGATVSRFSNLWKSYLEN 253
Cdd:PRK11854 582 AmePVWNGK-EFAPRLMLPLSLSYDHRVIDGADGARFITIINDRLSD 627
PRK11857 PRK11857
dihydrolipoamide acetyltransferase; Reviewed
 3-254 9.52e-54

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237002 [Multi-domain]  Cd Length: 306  Bit Score: 176.14  E-value: 9.52e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G         3 AEIMPPPPKPKDRTIPIPISKPPVFIGKdrTEPVKGFHKAMVKTMSAALK-IPHFGYCDEVDLTELVKLREELK-PIAFA 80
Cdd:PRK11857  50 AEAASVSSAQQAAKTAAPAAAPPKLEGK--REKVAPIRKAIARAMTNSWSnVAYVNLVNEIDMTKLWDLRKSVKdPVLKT 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        81 RGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQIRSIFEIATELNRLQKL 160
Cdd:PRK11857 128 EGVKLTFLPFIAKAILIALKEFPIFAAKYDEATSELVYPDTLNLGIAVDTEAGLMVPVIKNAQKLSIVEIAKEISRLAKA 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G       161 GSAGQLSTNDLIGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGTIKALPRFnEKGEVCKAQIMNVSWSADHRIIDGATV 240
Cdd:PRK11857 208 ARERKIKPDEMKGGSFTITNYGSVGSLYGVPVINYPELAIAGVGAIIDKAIV-KNGQIVAGKVMHLTVAADHRWIDGATI 286

                        250
                 ....*....|....
2II3_G       241 SRFSNLWKSYLENP 254
Cdd:PRK11857 287 GRFASRVKELLEKP 300
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 29-259 2.27e-47

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 165.05  E-value: 2.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G         29 GKDRTEPVKGFHKAMVKTMSAA-LKIPHFGYCDEVDLTELVKLREELKPIAFARGIKLSFMPFFLKAASLGLLQFPILNA 107
Cdd:TIGR01348 316 GEVEEVDMSRIRKISGANLTRNwTMIPHVTHFDKADITEMEAFRKQQNAAVEKEGVKLTVLHILMKAVAAALKKFPKFNA 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        108 SVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQIRSIFEIATELNRLQKLGSAGQLSTNDLIGGTFTLSNIGSIGGT 187
Cdd:TIGR01348 396 SLDLGGEQLILKKYVNIGVAVDTPNGLLVPVIKDVDRKGITELALELSDLAKKARDGKLTPDEMQGACFTISSLGGIGGT 475

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2II3_G        188 YAKPVILPPEVAIgaLGTIKAL--PRFNEKgEVCKAQIMNVSWSADHRIIDGATVSRFSNLWKSYLENPAFMLL 259
Cdd:TIGR01348 476 AFTPIVNAPEVAI--LGVSKSGmePVWNGK-EFEPRLMLPLSLSYDHRVIDGADAARFTTYICESLADIRRLLL 546
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 8-261 1.04e-46

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 160.62  E-value: 1.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G         8 PPPKPKDRTIPIPISKPPVFIGKDRTEPVKGFHK--AMVKTMSAALK--------IPHFgycDEVDLTELVKLREELKPI 77
Cdd:PTZ00144 160 PTPPAAAKPPEPAPAAKPPPTPVARADPRETRVPmsRMRQRIAERLKasqntcamLTTF---NECDMSALMELRKEYKDD 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        78 AFAR-GIKLSFMPFFLKAASLGLLQFPILNASVDENCqnITYKASHNIGIAMDTEQGLIVPNVKNVQIRSIFEIATELNR 156
Cdd:PTZ00144 237 FQKKhGVKLGFMSAFVKASTIALKKMPIVNAYIDGDE--IVYRNYVDISVAVATPTGLVVPVIRNCENKSFAEIEKELAD 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G       157 LQKLGSAGQLSTNDLIGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGTIKALP--RFNekgEVCKAQIMNVSWSADHRI 234
Cdd:PTZ00144 315 LAEKARNNKLTLEDMTGGTFTISNGGVFGSLMGTPIINPPQSAILGMHAIKKRPvvVGN---EIVIRPIMYLALTYDHRL 391

                        250       260
                 ....*....|....*....|....*..
2II3_G       235 IDGATVSRFSNLWKSYLENPAFMLLDL 261
Cdd:PTZ00144 392 IDGRDAVTFLKKIKDLIEDPARMLLDL 418
SucB_Actino TIGR02927
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model ...
 32-256 2.52e-44

2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase; This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).


Pssm-ID: 200219 [Multi-domain]  Cd Length: 579  Bit Score: 157.48  E-value: 2.52e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G         32 RTEPVKGFHKAMVKTMSAALKI-PHFGYCDEVDLTELVKLREELKPIAFAR-GIKLSFMPFFLKAASLGLLQFPILNASV 109
Cdd:TIGR02927 343 TTQKMNRIRQITADKTIESLQTsAQLTQVHEVDMTRVAALRARAKNDFLEKnGVNLTFLPFFVQAVTEALKAHPNVNASY 422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        110 DENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQIRSIFEIATELNRLQKLGSAGQLSTNDLIGGTFTLSNIGSIGGTYA 189
Cdd:TIGR02927 423 NAETKEVTYHDVEHVGIAVDTPRGLLVPVIHNAGDLSLPGLAKAINDLAARARDNKLKPDELSGGTFTITNIGSGGALFD 502

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2II3_G        190 KPVILPPEVAIGALGTIKALPRF--NEKG--EVCKAQIMNVSWSADHRIIDGATVSRFSNLWKSYLENPAF 256
Cdd:TIGR02927 503 TPILNPPQAAILGTGAIVKRPRVikDEDGgeSIAIRSVCYLPLTYDHRLVDGADAGRFLTTIKKRLEEGDF 573
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 61-261 1.27e-43

2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]


Pssm-ID: 273565 [Multi-domain]  Cd Length: 403  Bit Score: 152.20  E-value: 1.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G         61 EVDLTELVKLREELKPIAFAR-GIKLSFMPFFLKAASLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQGLIVPNV 139
Cdd:TIGR01347 205 EVDMSAVMELRKRYKEEFEKKhGVKLGFMSFFVKAVVAALKRFPEVNAEIDGD--DIVYKDYYDISVAVSTDRGLVVPVV 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        140 KNVQIRSIFEIATELNRLQKLGSAGQLSTNDLIGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGTIKALPrFNEKGEVC 219
Cdd:TIGR01347 283 RNADRMSFADIEKEIADLGKKARDGKLTLEDMTGGTFTITNGGVFGSLMSTPIINPPQSAILGMHGIKERP-VAVNGQIE 361

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
2II3_G        220 KAQIMNVSWSADHRIIDGATVSRFSNLWKSYLENPAFMLLDL 261
Cdd:TIGR01347 362 IRPMMYLALSYDHRLIDGKEAVTFLVTIKELLEDPRRLLLDL 403
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
61-261 8.87e-41

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 144.59  E-value: 8.87e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        61 EVDLTELVKLREELKPIAFAR-GIKLSFMPFFLKAASLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQGLIVPNV 139
Cdd:PRK05704 209 EVDMTPVMDLRKQYKDAFEKKhGVKLGFMSFFVKAVVEALKRYPEVNASIDGD--DIVYHNYYDIGIAVGTPRGLVVPVL 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G       140 KNVQIRSIFEIATELNRLQKLGSAGQLSTNDLIGGTFTLSNigsiGGTY----AKPVILPPEVAIgaLG--TIKALPrFN 213
Cdd:PRK05704 287 RDADQLSFAEIEKKIAELAKKARDGKLSIEELTGGTFTITN----GGVFgslmSTPIINPPQSAI--LGmhKIKERP-VA 359

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
2II3_G       214 EKGEVCKAQIMNVSWSADHRIIDGATVSRFSNLWKSYLENPAFMLLDL 261
Cdd:PRK05704 360 VNGQIVIRPMMYLALSYDHRIIDGKEAVGFLVTIKELLEDPERLLLDL 407
PDHac_trf_mito TIGR01349
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 7-259 1.93e-38

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273567 [Multi-domain]  Cd Length: 436  Bit Score: 139.16  E-value: 1.93e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G          7 PPPPKPKDRTIPIPISKPPVFIGKDRTEPVKGFHKAMVKTMSAALK-IPHFGYCDEVDLTELVKLREELKPIAFARgIKL 85
Cdd:TIGR01349 184 SANQQAAATTPATYPAAAPVSTGSYEDVPLSNIRKIIAKRLLESKQtIPHYYVSIECNVDKLLALRKELNAMASEV-YKL 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G         86 SFMPFFLKAASLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQGLIVPNVKNVQIRSIFEIATELNRLQKLGSAGQ 165
Cdd:TIGR01349 263 SVNDFIIKASALALREVPEANSSWTDN--FIRRYKNVDISVAVATPDGLITPIVRNADAKGLSTISNEIKDLAKRARNNK 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        166 LSTNDLIGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGTI--KALPRFNEKGEVCKAQIMNVSWSADHRIIDGATVSRF 243
Cdd:TIGR01349 341 LKPEEFQGGTFTISNLGMFGIKDFTAIINPPQACILAVGAVedVAVVDNDEEKGFAVASIMSVTLSCDHRVIDGAVGAEF 420

                         250
                  ....*....|....*.
2II3_G        244 SNLWKSYLENPAFMLL 259
Cdd:TIGR01349 421 LKSFKKYLENPIEMLL 436
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 7-261 2.71e-34

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 128.72  E-value: 2.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G         7 PPPPK---------PKDRTIPIPISKPPVFIGKDRTEPVKGFhkAMVKTMsaalkiphfgycDEVDLTELVKLREELKPI 77
Cdd:PLN02226 216 PPPPKqsakepqlpPKERERRVPMTRLRKRVATRLKDSQNTF--ALLTTF------------NEVDMTNLMKLRSQYKDA 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        78 AFAR-GIKLSFMPFFLKAASLGLLQFPILNASVDENcqNITYKASHNIGIAMDTEQGLIVPNVKNVQIRSIFEIATELNR 156
Cdd:PLN02226 282 FYEKhGVKLGLMSGFIKAAVSALQHQPVVNAVIDGD--DIIYRDYVDISIAVGTSKGLVVPVIRGADKMNFAEIEKTING 359

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G       157 LQKLGSAGQLSTNDLIGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGTIKALPRFnEKGEVCKAQIMNVSWSADHRIID 236
Cdd:PLN02226 360 LAKKANEGTISIDEMAGGSFTVSNGGVYGSLISTPIINPPQSAILGMHSIVSRPMV-VGGSVVPRPMMYVALTYDHRLID 438

                        250       260
                 ....*....|....*....|....*
2II3_G       237 GATVSRFSNLWKSYLENPAFMLLDL 261
Cdd:PLN02226 439 GREAVYFLRRVKDVVEDPQRLLLDI 463
PLN02744 PLN02744
dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
 53-259 7.63e-28

dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex


Pssm-ID: 215397 [Multi-domain]  Cd Length: 539  Bit Score: 111.48  E-value: 7.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        53 IPHFGYCDEVDLTELVKLREELKPIAFARGIK-LSFMPFFLKAASLGLLQFPILNAS-VDENcqnITYKASHNIGIAMDT 130
Cdd:PLN02744 332 IPHYYLTVDTRVDKLMALRSQLNSLQEASGGKkISVNDLVIKAAALALRKVPQCNSSwTDDY---IRQYHNVNINVAVQT 408

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G       131 EQGLIVPNVKNVQIRSIFEIATELNRLQKLGSAGQLSTNDLIGGTFTLSNIGS-IGGTYAKPVILPPEVAIGALGTI--K 207
Cdd:PLN02744 409 ENGLYVPVVKDADKKGLSTIAEEVKQLAQKARENSLKPEDYEGGTFTVSNLGGpFGIKQFCAIINPPQSAILAVGSAekR 488

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
2II3_G       208 ALPRFNEkGEVCKAQIMNVSWSADHRIIDGATVSRFSNLWKSYLENPAFMLL 259
Cdd:PLN02744 489 VIPGSGP-DQYNFASFMSVTLSCDHRVIDGAIGAEWLKAFKGYIENPESMLL 539
PRK14843 PRK14843
dihydrolipoamide acetyltransferase; Provisional
 9-259 2.66e-27

dihydrolipoamide acetyltransferase; Provisional


Pssm-ID: 184847 [Multi-domain]  Cd Length: 347  Bit Score: 107.68  E-value: 2.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G         9 PPKPKDRTIPIPISKPPVfiGKDRTEPVKGFHKAMVKTMSAA-LKIPHFGYCDEVDLTELVKLREE-LKPIAFARGIKLS 86
Cdd:PRK14843  98 SPAQIEKVEEVPDNVTPY--GEIERIPMTPMRKVIAQRMVESyLTAPTFTLNYEVDMTEMLALRKKvLEPIMEATGKKTT 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        87 FMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQIRSIFEIATELNRLQKLGSAGQL 166
Cdd:PRK14843 176 VTDLLSLAVVKTLMKHPYINASLTEDGKTIITHNYVNLAMAVGMDNGLMTPVVYNAEKMSLSELVVAFKDVIGRTLDGKL 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G       167 STNDLIGGTFTLSNIGSIGGTYAKPVILPPEVAI-GALGTIKALPRFNekGEVCKAQIMNVSWSADHRIIDGATVSRFSN 245
Cdd:PRK14843 256 APSELQNSTFTISNLGMFGVQSFGPIINQPNSAIlGVSSTIEKPVVVN--GEIVIRPIMSLGLTIDHRVVDGMAGAKFMK 333

                        250
                 ....*....|....
2II3_G       246 LWKSYLENPAFMLL 259
Cdd:PRK14843 334 DLKELIETPISMLI 347
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 7-243 4.88e-12

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 65.68  E-value: 4.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G          7 PPPPKPKDRTIPIPISKPPVFIGKDRTEPVKGFHKAMVKTMSAALKIPhfgycdevdlTEL------VKLREELKPI--- 77
Cdd:PRK12270   91 AAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRGAAAAVAKNMDASLEVP----------TATsvravpAKLLIDNRIVinn 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G         78 --AFARGIKLSFMPFFLKAASLGLLQFPILNASVDE--NCQNITYKASHNIGIAMDTEQ-----GLIVPNVKNVQIRSIF 148
Cdd:PRK12270  161 hlKRTRGGKVSFTHLIGYALVQALKAFPNMNRHYAEvdGKPTLVTPAHVNLGLAIDLPKkdgsrQLVVPAIKGAETMDFA 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2II3_G        149 EIATELNRLQKLGSAGQLSTNDLIGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGTIKALPRFNEKGEVCKAQ-----I 223
Cdd:PRK12270  241 QFWAAYEDIVRRARDGKLTADDFQGTTISLTNPGGIGTVHSVPRLMKGQGAIIGVGAMEYPAEFQGASEERLAElgiskV 320

                         250       260
                  ....*....|....*....|
2II3_G        224 MNVSWSADHRIIDGATVSRF 243
Cdd:PRK12270  321 MTLTSTYDHRIIQGAESGEF 340
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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